期刊
FEBS LETTERS
卷 589, 期 24, 页码 3915-3920出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2015.11.002
关键词
Histone-derived antimicrobial peptide; Buforin; Parasin; Membrane translocation; Membrane permeabilization; Arginine
资金
- National Institute of Allergy and Infectious Diseases (NIH-NIAID) [R15AI079685]
- National Science Foundation [CHE-0922860, CHE-1005032]
- Sherman Fairchild Foundation
Translocation of cell-penetrating peptides is often promoted by increased content of arginine or other guanidinium groups. However, relatively little research has considered the role of these functional groups on antimicrobial peptide activity. This study compared the activity of three histone-derived antimicrobial peptides-buforin II, DesHDAP1, and parasin-with variants that contain only lysine or arginine cationic residues. These peptides operate via different mechanisms as parasin causes membrane permeabilization while buforin II and DesHDAP1 translocate into bacteria. For all peptides, antibacterial activity increased with increased arginine content. Higher arginine content increased permeabilization for parasin while it improved translocation for buforin II and DesHDAP1. These observations provide insight into the relative importance of arginine and lysine in these antimicrobial peptides. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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